Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

You’ve supercharged your research process with ACS and Mendeley!

STEP 1:
Click to create an ACS ID

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

MENDELEY PAIRING EXPIRED
Your Mendeley pairing has expired. Please reconnect
ACS Publications. Most Trusted. Most Cited. Most Read
An Optimized MALDI Mass Spectrometry Method for Improved Detection of Lysine/Arginine/Histidine Free Peptides

OR SEARCH CITATIONS

My Activity
Publications

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Proteome Res. 2008, 7, 11, 5062-5069
    Technical Note

    An Optimized MALDI Mass Spectrometry Method for Improved Detection of Lysine/Arginine/Histidine Free Peptides
    Click to copy article linkArticle link copied!

    View Author Information
    Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de la Recherche Scientifique (CNRS) UMR 7104, Institut National de la Santé et de la Recherche Médicale (INSERM) U596, Université Louis Pasteur de Strasbourg, Illkirch, France, and Laboratoire de Spectrométrie de Masse Bio-Organique (LSMBO), Institut Pluridisciplinaire Hubert Curien, Département des Sciences Analytiques, Centre National de la Recherche Scientifique (CNRS) UMR7178, Université Louis Pasteur de Strasbourg, Strasbourg, France
    * To whom correspondence should be addressed. E-mail: [email protected]. Fax: 33 (0) 390242781.
    †Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université Louis Pasteur de Strasbourg.
    ‡Laboratoire de Spectrométrie de Masse Bio-Organique (LSMBO), Université Louis Pasteur de Strasbourg.
    #These authors equally contributed to this work.
    Other Access OptionsSupporting Information (1)

    Journal of Proteome Research

    Cite this: J. Proteome Res. 2008, 7, 11, 5062–5069
    Click to copy citationCitation copied!
    https://doi.org/10.1021/pr800276n
    Published October 16, 2008
    Copyright © 2008 American Chemical Society
    Request reuse permissions

    Abstract

    Click to copy section linkSection link copied!
    Abstract Image

    Transcription factors and their regulators possess “basic amino acid free domains” which modulate transcriptional gene activation. We aimed at optimizing a MALDI mass spectrometry (MS) analytical method for the characterization of such domains after protein enzymatic digestion. A panel of recombinant transcription factors with different basic residue contents was proteolytically digested with the Asp-N endoprotease and resulting peptide mixtures were analyzed by MALDI-MS with α-cyano-4-hydroxy-cinnamic acid (CHCA) and 2,5-dihydroxybenzoic acid (DHB) as matrix. We found that peptides without lysine, arginine, histidine (Lys/Arg/His free peptides) were efficiently detected in the positive ion mode only when using DHB. These findings proved to be very useful for two different targeted proteomic applications. Indeed, the MALDI-MS/MS identification of the CARM1 proteolytic cleavage site, which happens in a Lys/Arg/His free domain, could only be achieved using the DHB matrix. Moreover, in routine proteomic analyses, the detection efficiency of Lys/Arg/His free C-terminal peptides of two-dimensional gel separated proteins was strongly enhanced when DHB was used instead of CHCA.

    Copyright © 2008 American Chemical Society

    Subjects

    what are subjects

    Keywords

    what are keywords

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Supporting Information

    Click to copy section linkSection link copied!

    Table 1S showing effect of acidic (CHCA, DHB) and nonacidic (THAP, ATT) matrix compounds on the detection of PPARαAB Lys/Arg/His free peptides in positive (MH+) and negative ion mode (MH−) MALDI-MS analyses and Figure 1S showing the 1D gel of the 28-560 CARM1 purified recombinant protein and aminoacidic sequence of the initially expressed CARM1 recombinant protein. This material is available free of charge via the Internet at http://pubs.acs.org.

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 9 publications.

    1. Kjell Sergeant, Carla Pinheiro, Jean-François Hausman, Cândido Pinto Ricardo and Jenny Renaut . Taking Advantage of Nonspecific Trypsin Cleavages for the Identification of Seed Storage Proteins in Cereals. Journal of Proteome Research 2009, 8 (6) , 3182-3190. https://doi.org/10.1021/pr801093f
    2. Debabrata Chakraborty, Sourav Bej, Rupak Chatterjee, Priyabrata Banerjee, Asim Bhaumik. A new phosphonate based Mn-MOF in recognising arginine over lysine in aqueous medium and other bio-fluids with “Sepsis” disease remediation. Chemical Engineering Journal 2022, 446 , 136916. https://doi.org/10.1016/j.cej.2022.136916
    3. Tianran Wang, Qidan Pang, Zhipu Tong, Hanyue Xiang, Nao Xiao. A hydrazone-based spectroscopic off-on probe for sensing of basic arginine and lysine. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2021, 258 , 119824. https://doi.org/10.1016/j.saa.2021.119824
    4. Sebastian Tanco, Kris Gevaert, Petra Van Damme. C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini. PROTEOMICS 2015, 15 (5-6) , 903-914. https://doi.org/10.1002/pmic.201400301
    5. Martin L. Biniossek, Oliver Schilling. Enhanced identification of peptides lacking basic residues by LC‐ESI‐MS/MS analysis of singly charged peptides. PROTEOMICS 2012, 12 (9) , 1303-1309. https://doi.org/10.1002/pmic.201100569
    6. David da Silva, Thierry Wasselin, Vincent Carré, Patrick Chaimbault, Lina Bezdetnaya, Benoît Maunit, Jean‐François Muller. Evaluation of combined matrix‐assisted laser desorption/ionization time‐of‐flight and matrix‐assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry experiments for peptide mass fingerprinting analysis. Rapid Communications in Mass Spectrometry 2011, 25 (13) , 1881-1892. https://doi.org/10.1002/rcm.5057
    7. Thierry Rabilloud, Mireille Chevallet, Sylvie Luche, Cécile Lelong. Two-dimensional gel electrophoresis in proteomics: Past, present and future. Journal of Proteomics 2010, 73 (11) , 2064-2077. https://doi.org/10.1016/j.jprot.2010.05.016
    8. Chantal Sellier, Frédérique Rau, Yilei Liu, Flora Tassone, Renate K Hukema, Renata Gattoni, Anne Schneider, Stéphane Richard, Rob Willemsen, David J Elliott, Paul J Hagerman, Nicolas Charlet-Berguerand. Sam68 sequestration and partial loss of function are associated with splicing alterations in FXTAS patients. The EMBO Journal 2010, 29 (7) , 1248-1261. https://doi.org/10.1038/emboj.2010.21
    9. . Current literature in mass spectrometry. Journal of Mass Spectrometry 2009, 848-859. https://doi.org/10.1002/jms.1490
    Download PDF
    Go to Journal of Proteome Research
    Get e-Alerts
    Get e-Alerts

    Journal of Proteome Research

    Cite this: J. Proteome Res. 2008, 7, 11, 5062–5069
    Click to copy citationCitation copied!
    https://doi.org/10.1021/pr800276n
    Published October 16, 2008
    Copyright © 2008 American Chemical Society
    Request reuse permissions

    Article Views

    759

    Altmetric

    -

    Citations

    9
    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.